| pubmed-article:284333 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C0001492 | lld:lifeskim |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C0011485 | lld:lifeskim |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C0815047 | lld:lifeskim |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C1412327 | lld:lifeskim |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:284333 | lifeskim:mentions | umls-concept:C0332324 | lld:lifeskim |
| pubmed-article:284333 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:284333 | pubmed:dateCreated | 1979-5-26 | lld:pubmed |
| pubmed-article:284333 | pubmed:abstractText | Partially purified adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] from bovine brain cortex was fractionated into two separate forms by calcium-dependent regulatory protein (CDR)-Sepharose affinity chromatography. The major form of the enzyme, comprising approximately 80% of the applied activity, did not bind to the affinity column in the presence of Ca2+ and was insensitive to the CDR. Approximately 20% of adenylate cyclase activity was absorbed to CDR-Sepharose in the presence of Ca2+. This activity was stimulated by Ca2+ and CDR. This study directly demonstrates that brain cortex contains Ca2+-CDR-sensitive and -insensitive forms of adenylate cyclase and indicates that CDR-Sepharose may be a useful tool for purification of adenylate cyclase. The Ca2+ -stimulated adenylate cyclase was purified at least 55-fold with a 13% yield. | lld:pubmed |
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| pubmed-article:284333 | pubmed:language | eng | lld:pubmed |
| pubmed-article:284333 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:284333 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:284333 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:284333 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:284333 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:284333 | pubmed:author | pubmed-author:StoryD FDF | lld:pubmed |
| pubmed-article:284333 | pubmed:author | pubmed-author:WestcottK RKR | lld:pubmed |
| pubmed-article:284333 | pubmed:author | pubmed-author:La PorteD CDC | lld:pubmed |
| pubmed-article:284333 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:284333 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:284333 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:284333 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:284333 | pubmed:pagination | 204-8 | lld:pubmed |
| pubmed-article:284333 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:284333 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:284333 | pubmed:articleTitle | Resolution of adenylate cyclase sensitive and insensitive to Ca2+ and calcium-dependent regulatory protein (CDR) by CDR-sepharose affinity chromatography. | lld:pubmed |
| pubmed-article:284333 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:284333 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:284333 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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